FOG1_MOUSE - dbPTM
FOG1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FOG1_MOUSE
UniProt AC O35615
Protein Name Zinc finger protein ZFPM1
Gene Name Zfpm1
Organism Mus musculus (Mouse).
Sequence Length 995
Subcellular Localization Nucleus .
Protein Description Transcription regulator that plays an essential role in erythroid and megakaryocytic cell differentiation. Essential cofactor that acts via the formation of a heterodimer with transcription factors of the GATA family GATA1, GATA2 and GATA3. Such heterodimer can both activate or repress transcriptional activity, depending on the cell and promoter context. The heterodimer formed with GATA proteins is essential to activate expression of genes such as NFE2, ITGA2B, alpha- and beta-globin, while it represses expression of KLF1. May be involved in regulation of some genes in gonads. May also be involved in cardiac development, in a non-redundant way with ZFPM2/FOG2..
Protein Sequence MSRRKQSNPRQIKRSLRDMEAGEEAKAMDSSPKEQEAPDPEAPAIEEPPSPPREDVSPPAVPAPPESPEDPEDMEGQELEMRPQDEEKEEKEEEAAMASPWSGPEELELALQDGQRCVRARLSLTEGLSWGPFYGSIQTRALSPEREEPGPAVTLMVDESCWLRMLPQVLTEEAANSEIYRKDDALWCRVTKVVPSGGLLYVRLVTEPHGAPRHPVQEPVEPGGLAPVHTDIQLLPQQAGMASILATAVINKDVFPCKDCGIWYRSERNLQAHLLYYCASRQRAGSPVSATEEKPKETYPNERVCPFPQCRKSCPSASSLEIHMRSHSGERPFVCLICLSAFTTKANCERHLKVHTDTLSGVCHNCGFISTTRDILYSHLVTNHMVCQPGSKGEIYSPGAGHPAAKLPPDSLAGFQQHSLMHSPLVPADKAPTPSSGLDSKAEVTNGETRVPPQNGGSSESPAAPRTIKVEAAEEPEATRASGPGEPGPQAPSRTPSPHSPNPVRVKTELSSPTPGSSPGPGELTMAGTLFLPQYVFSPDAGTTTVPTAPQASEILAKMSELVHNRLQQGAGSSGAAGTPTGLFSGTKGATCFECEITFNNINNFYVHKRLYCSGRRAPEDPPTVRRPKAATGPARAPAGAAAEPDPSRSSPGPGPREEEASGTTTPEAEAAGRGSEGSQSPGSSVDDAEDDPSRTLCEACNIRFSRHETYTVHKRYYCASRHDPPPRRPPAPTTAPGPAAPALTAPPVRTRRRRKLYELPAAGAPPPAAGPAPVPVVPSPTAELPSSPRPGSASAGPAPALSPSPVPDGPIDLSKRPRRQSPDAPTALPALADYHECTACRVSFHSLEAYLAHKKYSCPAAPLRTTALCPYCPPNGRVRGDLVEHLRQAHGLQVAKPAASPGAEPRTPAERAPRDSPDGRAPRSPSPAPENTPSDPADQGARTPSKGPPAPAPAPGGGGGHRYCRLCNIRFSSLSTFIAHKKYYCSSHAAEHVK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
7Phosphorylation-MSRRKQSNPRQIKR
-CCCCCCCCHHHHHH		52.41-
50PhosphorylationPAIEEPPSPPREDVS
CCCCCCCCCCCCCCC		59.2530482847
99PhosphorylationEEEAAMASPWSGPEE
HHHHHHHCCCCCHHH		17.5130482847
143PhosphorylationSIQTRALSPEREEPG
CEECCCCCCCCCCCC		24.5921082442
154PhosphorylationEEPGPAVTLMVDESC
CCCCCCEEEEECCHH		15.9623984901
286PhosphorylationASRQRAGSPVSATEE
HHHCCCCCCCCCCCC		22.5727087446
289PhosphorylationQRAGSPVSATEEKPK
CCCCCCCCCCCCCCC		32.6226160508
291PhosphorylationAGSPVSATEEKPKET
CCCCCCCCCCCCCCC		36.8523984901
396PhosphorylationPGSKGEIYSPGAGHP
CCCCCCCCCCCCCCC		12.4328066266
397PhosphorylationGSKGEIYSPGAGHPA
CCCCCCCCCCCCCCH		23.6326643407
419PhosphorylationLAGFQQHSLMHSPLV
HCHHHHHCCCCCCCC		24.0526643407
423PhosphorylationQQHSLMHSPLVPADK
HHHCCCCCCCCCCCC		13.1326643407
433PhosphorylationVPADKAPTPSSGLDS
CCCCCCCCCCCCCCC		40.4328066266
435PhosphorylationADKAPTPSSGLDSKA
CCCCCCCCCCCCCCC		39.2428066266
436PhosphorylationDKAPTPSSGLDSKAE
CCCCCCCCCCCCCCE		44.5728066266
458PhosphorylationVPPQNGGSSESPAAP
CCCCCCCCCCCCCCC		32.1230482847
461PhosphorylationQNGGSSESPAAPRTI
CCCCCCCCCCCCCEE		23.0630482847
469SumoylationPAAPRTIKVEAAEEP
CCCCCEEEEEECCCC		33.15-
479PhosphorylationAAEEPEATRASGPGE
ECCCCHHHCCCCCCC		25.7123375375
482PhosphorylationEPEATRASGPGEPGP
CCHHHCCCCCCCCCC		42.0828066266
493PhosphorylationEPGPQAPSRTPSPHS
CCCCCCCCCCCCCCC		52.3725521595
495PhosphorylationGPQAPSRTPSPHSPN
CCCCCCCCCCCCCCC		32.2425521595
497PhosphorylationQAPSRTPSPHSPNPV
CCCCCCCCCCCCCCC		34.3325521595
500PhosphorylationSRTPSPHSPNPVRVK
CCCCCCCCCCCCEEE		29.7425521595
507SumoylationSPNPVRVKTELSSPT
CCCCCEEEEEECCCC		26.22-
574PhosphorylationLQQGAGSSGAAGTPT
HHHCCCCCCCCCCCC		31.3728066266
579PhosphorylationGSSGAAGTPTGLFSG
CCCCCCCCCCCCCCC		16.9828066266
581PhosphorylationSGAAGTPTGLFSGTK
CCCCCCCCCCCCCCC		46.4828066266
624PhosphorylationRAPEDPPTVRRPKAA
CCCCCCCCCCCCCCC		31.8430482847
648PhosphorylationAAAEPDPSRSSPGPG
CCCCCCCCCCCCCCC		52.7723684622
650PhosphorylationAEPDPSRSSPGPGPR
CCCCCCCCCCCCCCC		45.2625521595
651PhosphorylationEPDPSRSSPGPGPRE
CCCCCCCCCCCCCCH		32.5325521595
662PhosphorylationGPREEEASGTTTPEA
CCCHHHHCCCCCHHH		39.7026643407
664PhosphorylationREEEASGTTTPEAEA
CHHHHCCCCCHHHHH		25.6326643407
665PhosphorylationEEEASGTTTPEAEAA
HHHHCCCCCHHHHHC		43.8326643407
666PhosphorylationEEASGTTTPEAEAAG
HHHCCCCCHHHHHCC		20.9717203969
676PhosphorylationAEAAGRGSEGSQSPG
HHHCCCCCCCCCCCC		37.1125266776
679PhosphorylationAGRGSEGSQSPGSSV
CCCCCCCCCCCCCCC		24.3527087446
681PhosphorylationRGSEGSQSPGSSVDD
CCCCCCCCCCCCCCC		32.6925521595
684PhosphorylationEGSQSPGSSVDDAED
CCCCCCCCCCCCCCC		30.4925521595
685PhosphorylationGSQSPGSSVDDAEDD
CCCCCCCCCCCCCCC		35.1727087446
788PhosphorylationPTAELPSSPRPGSAS
CCCCCCCCCCCCCCC		24.0023384938
793PhosphorylationPSSPRPGSASAGPAP
CCCCCCCCCCCCCCC		23.0228066266
795PhosphorylationSPRPGSASAGPAPAL
CCCCCCCCCCCCCCC		35.1428066266
803PhosphorylationAGPAPALSPSPVPDG
CCCCCCCCCCCCCCC		25.9928066266
805PhosphorylationPAPALSPSPVPDGPI
CCCCCCCCCCCCCCC		34.8428066266
822PhosphorylationSKRPRRQSPDAPTAL
CCCCCCCCCCCCCHH		23.9627087446
827PhosphorylationRQSPDAPTALPALAD
CCCCCCCCHHHHHHC		42.4127149854
901PhosphorylationQVAKPAASPGAEPRT
CCCCCCCCCCCCCCC		26.4426745281
917PhosphorylationAERAPRDSPDGRAPR
HHHCCCCCCCCCCCC		26.6027087446
925PhosphorylationPDGRAPRSPSPAPEN
CCCCCCCCCCCCCCC		28.7725521595
927PhosphorylationGRAPRSPSPAPENTP
CCCCCCCCCCCCCCC		34.6325521595
933PhosphorylationPSPAPENTPSDPADQ
CCCCCCCCCCCHHHC		23.6222817900
935PhosphorylationPAPENTPSDPADQGA
CCCCCCCCCHHHCCC		54.9421183079
944PhosphorylationPADQGARTPSKGPPA
HHHCCCCCCCCCCCC		31.2319854140
946PhosphorylationDQGARTPSKGPPAPA
HCCCCCCCCCCCCCC		50.0221183079
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of FOG1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FOG1_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of FOG1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GATA1_MOUSEGata1physical
19654328
CTBP1_MOUSECtbp1physical
19654328
CTBP2_MOUSECtbp2physical
19654328
KDM1A_MOUSEKdm1aphysical
19654328
MTA1_MOUSEMta1physical
19654328
MTA2_MOUSEMta2physical
19654328
RBBP7_MOUSERbbp7physical
19654328
CTIP_MOUSERbbp8physical
19654328
HDAC2_MOUSEHdac2physical
19654328
HDAC1_MOUSEHdac1physical
19654328
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FOG1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-497; SER-500; SER-651;SER-925 AND SER-927, AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-666, AND MASSSPECTROMETRY.

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